Architecture of the mammalian mechanosensitive Piezo1 channel

Jingpeng Ge, Wanqiu Li, Qiancheng Zhao, Ningning Li, Maofei Chen, Peng Zhi, Ruochong Li, Ning Gao (), Bailong Xiao () and Maojun Yang ()
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Jingpeng Ge: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University
Wanqiu Li: Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University
Qiancheng Zhao: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University
Ningning Li: Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University
Maofei Chen: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University
Peng Zhi: School of Medicine, Tsinghua University
Ruochong Li: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University
Ning Gao: Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University
Bailong Xiao: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University
Maojun Yang: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University

Nature, 2015, vol. 527, issue 7576, 64-69

Abstract: Abstract Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have remained unknown. Here we determine the cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezo1 (Piezo1) at a resolution of 4.8 Å. Piezo1 forms a trimeric propeller-like structure (about 900 kilodalton), with the extracellular domains resembling three distal blades and a central cap. The transmembrane region has 14 apparently resolved segments per subunit. These segments form three peripheral wings and a central pore module that encloses a potential ion-conducting pore. The rather flexible extracellular blade domains are connected to the central intracellular domain by three long beam-like structures. This trimeric architecture suggests that Piezo1 may use its peripheral regions as force sensors to gate the central ion-conducting pore.

Date: 2015
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DOI: 10.1038/nature15247

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